ID D4K750_9FIRM Unreviewed; 203 AA.
AC D4K750;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000313|EMBL:CBL00663.1};
DE EC=2.3.1.51 {ECO:0000313|EMBL:CBL00663.1};
GN ORFNames=FPR_02110 {ECO:0000313|EMBL:CBL00663.1};
OS Faecalibacterium prausnitzii SL3/3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL00663.1, ECO:0000313|Proteomes:UP000007059};
RN [1] {ECO:0000313|EMBL:CBL00663.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00663.1,
RC ECO:0000313|Proteomes:UP000007059};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL00663.1, ECO:0000313|Proteomes:UP000007059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL3/3 {ECO:0000313|EMBL:CBL00663.1,
RC ECO:0000313|Proteomes:UP000007059};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC by incorporating acyl moiety at the 2 position.
CC {ECO:0000256|ARBA:ARBA00037183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141};
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DR EMBL; FP929046; CBL00663.1; -; Genomic_DNA.
DR AlphaFoldDB; D4K750; -.
DR KEGG; fpa:FPR_02110; -.
DR PATRIC; fig|657322.3.peg.730; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_4_5_9; -.
DR Proteomes; UP000007059; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF60; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE LPAT1, CHLOROPLASTIC; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CBL00663.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:CBL00663.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..151
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 203 AA; 23048 MW; 7017AA16F46129B9 CRC64;
MVLYYILVPL AWLVWHIGFR IRVEGRENLK KVQTKGYILA PTHVSAIDPV FIVVTRWGRR
MVVFAKKELF EINAFLTWFF RCCGGVCVRG TKDEMAVISQ TVEACKQGKT LLIFPEGTRE
KEGKLLPPKS GLFVIAAEAG VDVVPCRILY DTPDGRMHLF CKVRVIYGEP MPAAQFAMEG
RRDTKKLRAN KQALLEAWEK MGA
//
